Evidence map›Paper›PMID 25862830›Full record

ReviewAmerican journal of physiology. Heart and circulatory physiology2015

Protein assemblies of sodium and inward rectifier potassium channels control cardiac excitability and arrhythmogenesis.

B Cicero Willis, Daniela Ponce-Balbuena, José Jalife

Abstract readReview
In one paragraph

Review in American journal of physiology. Heart and circulatory physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Extracellular Kir2.1Circulation research · 2024
    Article
  4. Article
  5. Extracellular cysteine disulfide bond break at Cys122 disrupts PIPbioRxiv : the preprint server for biology · 2023
    Article
  6. Article
  7. Review
  8. Review
  9. Article
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Kir2.1 & NaCirculation research · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 2 countries.

B Cicero WillisDepartment of Internal Medicine and Center for Arrhythmia Research, University of Michigan, Ann Arbor, Michigan; and.
Daniela Ponce-BalbuenaDepartment of Internal Medicine and Center for Arrhythmia Research, University of Michigan, Ann Arbor, Michigan; and.
José JalifeDepartment of Internal Medicine and Center for Arrhythmia Research, University of Michigan, Ann Arbor, Michigan; and Centro Nacional de Investigaciones Cardiovasculares, Madrid, Spain jjalife@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Intermolecular Interactions of NaV1.5 and Kir2.1 In Ion Channel DiseasesR01HL122352 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BERENFELD, OMER · 2015 to 2018
$1.9M
NHLBI NIH HHS HL122352NHLBI NIH HHS R01 HL122352
6 · The paper itself

Abstract

The understanding of how cardiac ion channels function in the normal and the diseased heart has greatly increased over the last four decades thanks to the advent of patch-clamp technology and, more recently, the emergence of genetics, as well as cellular and molecular cardiology. However, our knowledge of how these membrane-embedded proteins physically interact with each other within macromolecular complexes remains incomplete. This review focuses on how the main cardiac inward sodium channel (NaV1.5) and the strong inward rectifier potassium channel (Kir2.1) function within macromolecular complexes to control cardiac excitability. It has become increasingly clear that these two important ion channel proteins physically interact with multiple other protein partners and with each other from early stages of protein trafficking and targeting through membrane anchoring, recycling, and degradation. Recent findings include compartmentalized regulation of NaV1.5 channel expression and function through a PDZ (postsynaptic density protein, Drosophila disc large tumor suppressor, and zonula occludens-1 protein) domain-binding motif, and interaction of caveolin-3 with Kir2.1 and ankyrin-G as a molecular platform for NaV1.5 signaling. At the cardiomyocyte membrane, NaV1.5 and Kir2.1 interact through at least two distinct PDZ domain-scaffolding proteins (synapse-associated protein-97 and α1-syntrophin), thus modulating reciprocally their cell-surface expression at two different microdomains. Emerging evidence also shows that inheritable mutations in plakophilin-2, ankyrin-G, dystrophin, syntrophin, synapse-associated protein-97, and caveolin-3, among others, modify functional expression and/or localization in the cardiac cell of NaV1.5, Kir2.1 or both to give rise to arrhythmogenic diseases. Unveiling the mechanistic underpinnings of macromolecular interactions should increase our understanding of inherited and acquired arrhythmogenic cardiac diseases and may lead to advances in therapy.

Indexed as

Action PotentialsAnimalsArrhythmias, CardiacHumansMembrane MicrodomainsMultiprotein ComplexesMyocytes, CardiacNAV1.5 Voltage-Gated Sodium ChannelPotassium Channels, Inwardly RectifyingSignal TransductionKir2.1 channelMultiprotein ComplexesNAV1.5 Voltage-Gated Sodium ChannelPotassium Channels, Inwardly RectifyingKir2.1macromolecular complexNaV1.5SAP97syntrophin

Identifiers

PMID25862830
PMCPMC4469872
OpenAlexW2079694201

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.